Hsp90 molecular chaperone: structure, functions and participation in the cardio-vascular pathologies
This review is devoted to analysis of structural and functional properties of molecular chaperon Hsp90. Hsp90 are highly widespread family of heat shock proteins . Protein is found in eubacteria and all branches of eukarya, but it is apparently absent in archaea. It is one of key regulators of numer...
Збережено в:
| Дата: | 2009 |
|---|---|
| Автор: | |
| Формат: | Стаття |
| Мова: | English |
| Опубліковано: |
Інститут молекулярної біології і генетики НАН України
2009
|
| Назва видання: | Вiopolymers and Cell |
| Теми: | |
| Онлайн доступ: | http://dspace.nbuv.gov.ua/handle/123456789/153005 |
| Теги: |
Додати тег
Немає тегів, Будьте першим, хто поставить тег для цього запису!
|
| Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Цитувати: | Hsp90 molecular chaperone: structure, functions and participation in the cardio-vascular pathologies / I.V. Kroupskaya // Вiopolymers and Cell. — 2009. — Т. 25, № 5. — С. 372-383. — Бібліогр.: 61 назв. — англ, рос. |
Репозитарії
Digital Library of Periodicals of National Academy of Sciences of Ukraine| Резюме: | This review is devoted to analysis of structural and functional properties of molecular chaperon Hsp90. Hsp90 are highly widespread family of heat shock proteins . Protein is found in eubacteria and all branches of eukarya, but it is apparently absent in archaea. It is one of key regulators of numerous signalling pathways, cell growth and development, apoptosis, induction of autoimmunity and progression of heart failure. The full functional activity of Hsp90 shows up in a complex with other molecular chaperones and co-chaperones. Molecular interactions between chaperones, different signaling proteins and protein-partners are highly crucial for the normal functioning of signaling pathways and its destruction are causes the alteration of cell physiology up to its death. |
|---|